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- Title
New insights in the ϕ29 terminal protein DNA-binding and host nucleoid localization functions.
- Authors
Holguera, Isabel; Redrejo‐Rodríguez, Modesto; Salas, Margarita; Muñoz‐Espín, Daniel
- Abstract
Protein-primed DNA replication constitutes a strategy to initiate viral DNA synthesis in a variety of prokaryotic and eukaryotic organisms. Although the main function of viral terminal proteins ( TPs) is to provide a free hydroxyl group to start initiation of DNA replication, there are compelling evidences that TPs can also play other biological roles. In the case of Bacillus subtilis bacteriophage ϕ29, the N-terminal domain of the TP organizes viral DNA replication at the bacterial nucleoid being essential for an efficient phage DNA replication, and it contains a nuclear localization signal ( NLS) that is functional in eukaryotes. Here we provide information about the structural properties of the ϕ29 TP N-terminal domain, which possesses sequence-independent DNA-binding capacity, and dissect the amino acid residues important for its biological function. By mutating all the basic residues of the TP N-terminal domain we identify the amino acids responsible for its interaction with the B. subtilis genome, establishing a correlation between the capacity of DNA-binding and nucleoid localization of the protein. Significantly, these residues are important to recruit the DNA polymerase at the bacterial nucleoid and, subsequently, for an efficient phage DNA replication.
- Subjects
DNA-binding proteins; DNA replication; NUCLEOIDS; C-terminal binding proteins; EUKARYOTIC cells; HYDROXYL group; VIRAL genetics
- Publication
Molecular Microbiology, 2014, Vol 91, Issue 2, p232
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/mmi.12456